A novel member of the RING finger family, KRIP-1, associates with the KRAB-A transcriptional repressor domain of zinc finger proteins

Kim, Sung‐Su; Chen, Ming-Fong; O’Leary, Eileen; Witzgall, Ralph; Vidal, Marc; Bonventre, Joseph V.

doi:10.1073/pnas.93.26.15299

Cited by 264 publications

(204 citation statements)

References 32 publications

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“…We recently identifed KAP1 [12], a co-repressor of the Kruppel-associated box (KRAB)-domain-containing zinc finger proteins [13][14][15] as a protein that interacts specifically with STAT1, STAT3, STAT4 and STAT6. KAP1 can recruit and coordinate many components involved in gene silencing.…”

Section: Treatment Of Cells With Ifn Induces the Activation Of Jak-stmentioning

confidence: 99%

KAP1 regulates type I interferon/STAT1-mediated IRF-1 gene expression

Kamitani

Ohbayashi

Ikeda

et al. 2008

Biochemical and Biophysical Research Communications

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Signal transducers and activators of transcription (STATs) mediate cell proliferation, differentiation, and survival in immune responses, hematopoiesis, neurogenesis, and other biological processes.Recently, we showed that KAP1 is a novel STAT-binding partner that regulates STAT3-mediated transactivation. KAP1 is a universal corepressor protein for the KRAB zinc finger protein superfamily of transcriptional repressors. In this study, we found KAP1-dependent repression of interferon (IFN) /STAT1-mediated signaling. We also demonstrated that endogenous KAP1 associates with endogenous STAT1 in vivo. Importantly, a small-interfering RNA-mediated reduction in KAP1 expression enhanced IFN-induced STAT1-dependent IRF-1 gene expression.These results indicate that KAP1 may act as an endogenous regulator of the IFN/STAT1 signaling pathway.

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Section: Treatment Of Cells With Ifn Induces the Activation Of Jak-stmentioning

confidence: 99%

KAP1 regulates type I interferon/STAT1-mediated IRF-1 gene expression

Kamitani

Ohbayashi

Ikeda

et al. 2008

Biochemical and Biophysical Research Communications

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“…However, they also bind to several other proteins (e.g. Kim et al 28 and El-Husseini et al 29 ). To elucidate the function of EBBP we performed a yeast twohybrid screen to search for proteins, which bind to its RFP domain.…”

Section: Ebbp Interacts With Proil-1bmentioning

confidence: 99%

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

et al. 2006

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The estrogen-responsive B box protein (EBBP) and Pyrin belong to a family of structurally related proteins. While mutations in the pyrin gene cause an autoinflammatory disease, the biological function of EBBP is unknown. In this study, we identified the proinflammatory cytokine interleukin1b (IL-1b) as an EBBP-binding partner. Furthermore, caspase-1 and NACHT, LRR and Pyrin domain containing protein (NALP) 1, two components of the recently identified inflammasome, a platform for the activation of caspase-1, also interact with EBBP. These proteins bind to the RFP domain of EBBP, suggesting that this domain of so far unknown function is an important protein-binding domain. EBBP was secreted in a caspase-1-dependent manner from cultured cells, and its secretion was enhanced by IL-1b. Vice versa, endogenous and overerexpressed EBBP increased IL-1b secretion. These results provide evidence for a role of EBBP in innate immunity by enhancing the alternative secretion pathway of IL-1b.

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“…KAP1/TIF1b was initially identified as a corepressor for the Kruppel-associated box-domain-containing zincfinger proteins (Friedman et al, 1996;Kim et al, 1996;Agata et al, 1999). KAP1 can recruit and coordinate many components involved in gene silencing.…”

mentioning

confidence: 99%

Physical and functional interactions between STAT3 and KAP1

et al. 2007

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Signal transducers and activators of transcription (STATs) mediate cell proliferation, differentiation and survival in immune responses, hematopoiesis, neurogenesis and other biological processes. For example, STAT3 has been reported to be constitutively activated in numerous cancer cells. To clarify the molecular mechanisms underlying the STAT activation, we performed yeast two-hybrid screening and identified KAP1/TIF1b as a novel STATbinding partner. KAP1 is a universal corepressor protein for the Kruppel-associated box zinc-finger protein superfamily of transcriptional repressors. We found endogenous KAP1 associated with endogenous STAT3 in vivo. Importantly, small-interfering RNA-mediated reduction of KAP1 expression enhanced interleukin (IL)-6-induced STAT3-dependent transcription and gene expression. Furthermore, reduction of KAP1 expression resulted in the marked accumulation of STAT3 phosphorylated on Ser727 in the nucleus, a modification that regulates its transcriptional activation. These results indicate that KAP1 may serve as a transcriptional regulator of the IL-6/STAT3 signaling pathway.

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A novel member of the RING finger family, KRIP-1, associates with the KRAB-A transcriptional repressor domain of zinc finger proteins

Cited by 264 publications

References 32 publications

KAP1 regulates type I interferon/STAT1-mediated IRF-1 gene expression

KAP1 regulates type I interferon/STAT1-mediated IRF-1 gene expression

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

Physical and functional interactions between STAT3 and KAP1

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